CRYBA1

Crystallin, beta A1
Identifiers
Symbols	CRYBA1 ; CRYB1
External IDs	Template:OMIM5 Template:MGI HomoloGene: 3815
Gene ontology Molecular function Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Crystallin, beta A1, also known as CRYBA1, is a human gene.

Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta acidic group member, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'.

Further reading

• Hulsebos TJ, Bijlsma EK, Geurts van Kessel AH; et al. (1991). "Direct assignment of the human beta B2 and beta B3 crystallin genes to 22q11.2----q12: markers for neurofibromatosis 2". Cytogenet. Cell Genet. 56 (3–4): 171–5. PMID 2055112.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hogg D, Tsui LC, Gorin M, Breitman ML (1986). "Characterization of the human beta-crystallin gene Hu beta A3/A1 reveals ancestral relationships among the beta gamma-crystallin superfamily". J. Biol. Chem. 261 (26): 12420–7. PMID 3745196.CS1 maint: Multiple names: authors list (link)
• Sparkes RS, Mohandas T, Heinzmann C; et al. (1986). "Assignment of a human beta-crystallin gene to 17cen-q23". Hum. Genet. 74 (2): 133–6. PMID 3770741.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Basti S, Hejtmancik JF, Padma T; et al. (1996). "Autosomal dominant zonular cataract with sutural opacities in a four-generation family". Am. J. Ophthalmol. 121 (2): 162–8. PMID 8623885.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Werten PJ, Carver JA, Jaenicke R, de Jong WW (1997). "The elusive role of the N-terminal extension of beta A3- and beta A1-crystallin". Protein Eng. 9 (11): 1021–8. PMID 8961355.CS1 maint: Multiple names: authors list (link)
• Lampi KJ, Ma Z, Shih M; et al. (1997). "Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens". J. Biol. Chem. 272 (4): 2268–75. PMID 8999933.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kannabiran C, Rogan PK, Olmos L; et al. (1998). "Autosomal dominant zonular cataract with sutural opacities is associated with a splice mutation in the betaA3/A1-crystallin gene". Mol. Vis. 4: 21. PMID 9788845.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Srivastava OP, Srivastava K (1999). "Characterization of a sodium deoxycholate-activatable proteinase activity associated with betaA3/A1-crystallin of human lenses". Biochim. Biophys. Acta. 1434 (2): 331–46. PMID 10525151.
• Graw J, Jung M, Löster J; et al. (2000). "Mutation in the betaA3/A1-crystallin encoding gene Cryba1 causes a dominant cataract in the mouse". Genomics. 62 (1): 67–73. doi:10.1006/geno.1999.5974. PMID 10585769.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Vanita , Sarhadi V, Reis A; et al. (2001). "A unique form of autosomal dominant cataract explained by gene conversion between beta-crystallin B2 and its pseudogene". J. Med. Genet. 38 (6): 392–6. PMID 11424921.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• MacCoss MJ, McDonald WH, Saraf A; et al. (2002). "Shotgun identification of protein modifications from protein complexes and lens tissue". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 7900–5. doi:10.1073/pnas.122231399. PMID 12060738.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Qi Y, Jia H, Huang S; et al. (2004). "A deletion mutation in the betaA1/A3 crystallin gene ( CRYBA1/A3) is associated with autosomal dominant congenital nuclear cataract in a Chinese family". Hum. Genet. 114 (2): 192–7. doi:10.1007/s00439-003-1049-7. PMID 14598164.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Reddy MA, Bateman OA, Chakarova C; et al. (2004). "Characterization of the G91del CRYBA1/3-crystallin protein: a cause of human inherited cataract". Hum. Mol. Genet. 13 (9): 945–53. doi:10.1093/hmg/ddh110. PMID 15016766.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ferrini W, Schorderet DF, Othenin-Girard P; et al. (2004). "CRYBA3/A1 gene mutation associated with suture-sparing autosomal dominant congenital nuclear cataract: a novel phenotype". Invest. Ophthalmol. Vis. Sci. 45 (5): 1436–41. PMID 15111599.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lapko VN, Cerny RL, Smith DL, Smith JB (2005). "Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation". Protein Sci. 14 (1): 45–54. doi:10.1110/ps.04738505. PMID 15576560.CS1 maint: Multiple names: authors list (link)
• Takata T, Oxford JT, Brandon TR, Lampi KJ (2007). "Deamidation alters the structure and decreases the stability of human lens betaA3-crystallin". Biochemistry. 46 (30): 8861–71. doi:10.1021/bi700487q. PMID 17616172.CS1 maint: Multiple names: authors list (link)
• Lu S, Zhao C, Jiao H; et al. (2007). "Two Chinese families with pulverulent congenital cataracts and deltaG91 CRYBA1 mutations". Mol. Vis. 13: 1154–60. PMID 17653060.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)